JP4348194B2 - ブドウ球菌溶解活性が増強された切断型リゾスタフィン分子 - Google Patents

ブドウ球菌溶解活性が増強された切断型リゾスタフィン分子 Download PDF

Info

Publication number: JP4348194B2
Authority: JP; Japan
Prior art keywords: lysostaphin; truncated; host cell; protein; recombinant
Prior art date: 2001-12-21
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Expired - Fee Related

Application number

JP2003579727A

Other languages

English (en)

Japanese (ja)

Other versions

JP2005519628A (ja

Inventor

スティンソン，ジェフリー，アール．

グリンバーグ，リオウボヴ

リーズ，アンドリュー

モンド，ジェームズ，ジェイ．

コカイ−クン，ジョン，エフ．

Original Assignee

バイオシネクサスインコーポレーテッド

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

2001-12-21

Filing date

2002-12-23

Publication date

2009-10-21

2002-12-23 Application filed by バイオシネクサスインコーポレーテッド filed Critical バイオシネクサスインコーポレーテッド

2005-07-07 Publication of JP2005519628A publication Critical patent/JP2005519628A/ja

2009-10-21 Application granted granted Critical

2009-10-21 Publication of JP4348194B2 publication Critical patent/JP4348194B2/ja

2022-12-23 Anticipated expiration legal-status Critical

Status Expired - Fee Related legal-status Critical Current

Links

108090000988 Lysostaphin Proteins 0.000 title claims abstract description 300
230000002101 lytic effect Effects 0.000 title 1
108020004414 DNA Proteins 0.000 claims abstract description 20
238000004519 manufacturing process Methods 0.000 claims abstract description 18
150000001413 amino acids Chemical class 0.000 claims description 24
238000000034 method Methods 0.000 claims description 23
108090000623 proteins and genes Proteins 0.000 claims description 21
102000053602 DNA Human genes 0.000 claims description 14
102000004169 proteins and genes Human genes 0.000 claims description 14
108010076504 Protein Sorting Signals Proteins 0.000 claims description 13
108091028043 Nucleic acid sequence Proteins 0.000 claims description 9
241000588724 Escherichia coli Species 0.000 claims description 8
239000008194 pharmaceutical composition Substances 0.000 claims description 8
229920001184 polypeptide Polymers 0.000 claims description 7
108090000765 processed proteins & peptides Proteins 0.000 claims description 7
102000004196 processed proteins & peptides Human genes 0.000 claims description 7
230000028327 secretion Effects 0.000 claims description 5
239000003937 drug carrier Substances 0.000 claims description 4
241000193386 Lysinibacillus sphaericus Species 0.000 claims description 3
125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 claims description 3
238000012258 culturing Methods 0.000 claims description 3
108700039691 Genetic Promoter Regions Proteins 0.000 claims description 2
230000002934 lysing effect Effects 0.000 claims description 2
230000001939 inductive effect Effects 0.000 claims 2
241000192129 Leuconostoc lactis Species 0.000 claims 1
238000002360 preparation method Methods 0.000 abstract description 22
208000015181 infectious disease Diseases 0.000 abstract description 20
108020004511 Recombinant DNA Proteins 0.000 abstract description 19
241000894006 Bacteria Species 0.000 abstract description 17
210000004027 cell Anatomy 0.000 description 50
238000003556 assay Methods 0.000 description 26
239000013612 plasmid Substances 0.000 description 26
239000000523 sample Substances 0.000 description 23
230000000694 effects Effects 0.000 description 20
239000000203 mixture Substances 0.000 description 20
241000191967 Staphylococcus aureus Species 0.000 description 16
108090000790 Enzymes Proteins 0.000 description 15
102000004190 Enzymes Human genes 0.000 description 15
235000001014 amino acid Nutrition 0.000 description 15
230000001580 bacterial effect Effects 0.000 description 15
238000010790 dilution Methods 0.000 description 15
239000012895 dilution Substances 0.000 description 15
229940088598 enzyme Drugs 0.000 description 15
238000006243 chemical reaction Methods 0.000 description 14
238000003752 polymerase chain reaction Methods 0.000 description 14
230000000844 anti-bacterial effect Effects 0.000 description 13
239000000969 carrier Substances 0.000 description 13
239000012634 fragment Substances 0.000 description 13
HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 12
239000003814 drug Substances 0.000 description 12
235000018102 proteins Nutrition 0.000 description 12
239000000047 product Substances 0.000 description 11
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
239000002609 medium Substances 0.000 description 10
125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 10
206010041925 Staphylococcal infections Diseases 0.000 description 9
239000008280 blood Substances 0.000 description 9
210000004369 blood Anatomy 0.000 description 9
229940079593 drug Drugs 0.000 description 9
239000000758 substrate Substances 0.000 description 9
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 8
241000295644 Staphylococcaceae Species 0.000 description 8
238000011534 incubation Methods 0.000 description 8
230000003834 intracellular effect Effects 0.000 description 8
238000000746 purification Methods 0.000 description 8
230000009467 reduction Effects 0.000 description 8
239000000243 solution Substances 0.000 description 8
229920001059 synthetic polymer Polymers 0.000 description 8
239000000872 buffer Substances 0.000 description 7
210000003928 nasal cavity Anatomy 0.000 description 7
239000002773 nucleotide Substances 0.000 description 7
125000003729 nucleotide group Chemical group 0.000 description 7
238000012163 sequencing technique Methods 0.000 description 7
238000000108 ultra-filtration Methods 0.000 description 7
CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 6
241001465754 Metazoa Species 0.000 description 6
230000000941 anti-staphylcoccal effect Effects 0.000 description 6
JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 6
108020004999 messenger RNA Proteins 0.000 description 6
229920005615 natural polymer Polymers 0.000 description 6
230000010076 replication Effects 0.000 description 6
238000011282 treatment Methods 0.000 description 6
241000283973 Oryctolagus cuniculus Species 0.000 description 5
229920002684 Sepharose Polymers 0.000 description 5
239000006161 blood agar Substances 0.000 description 5
210000002421 cell wall Anatomy 0.000 description 5
238000010367 cloning Methods 0.000 description 5
238000002474 experimental method Methods 0.000 description 5
239000013613 expression plasmid Substances 0.000 description 5
ZFKJVJIDPQDDFY-UHFFFAOYSA-N fluorescamine Chemical compound C12=CC=CC=C2C(=O)OC1(C1=O)OC=C1C1=CC=CC=C1 ZFKJVJIDPQDDFY-UHFFFAOYSA-N 0.000 description 5
239000000463 material Substances 0.000 description 5
230000008569 process Effects 0.000 description 5
239000011780 sodium chloride Substances 0.000 description 5
MINDHVHHQZYEEK-UHFFFAOYSA-N (E)-(2S,3R,4R,5S)-5-[(2S,3S,4S,5S)-2,3-epoxy-5-hydroxy-4-methylhexyl]tetrahydro-3,4-dihydroxy-(beta)-methyl-2H-pyran-2-crotonic acid ester with 9-hydroxynonanoic acid Natural products CC(O)C(C)C1OC1CC1C(O)C(O)C(CC(C)=CC(=O)OCCCCCCCCC(O)=O)OC1 MINDHVHHQZYEEK-UHFFFAOYSA-N 0.000 description 4
108091026890 Coding region Proteins 0.000 description 4
108020004705 Codon Proteins 0.000 description 4
102000010911 Enzyme Precursors Human genes 0.000 description 4
108010062466 Enzyme Precursors Proteins 0.000 description 4
239000004471 Glycine Substances 0.000 description 4
235000010469 Glycine max Nutrition 0.000 description 4
238000012408 PCR amplification Methods 0.000 description 4
241000191963 Staphylococcus epidermidis Species 0.000 description 4
230000015556 catabolic process Effects 0.000 description 4
239000003153 chemical reaction reagent Substances 0.000 description 4
239000000356 contaminant Substances 0.000 description 4
239000006071 cream Substances 0.000 description 4
238000005520 cutting process Methods 0.000 description 4
230000009089 cytolysis Effects 0.000 description 4
238000006731 degradation reaction Methods 0.000 description 4
239000013024 dilution buffer Substances 0.000 description 4
238000012377 drug delivery Methods 0.000 description 4
239000006167 equilibration buffer Substances 0.000 description 4
238000000855 fermentation Methods 0.000 description 4
230000004151 fermentation Effects 0.000 description 4
238000001914 filtration Methods 0.000 description 4
239000000499 gel Substances 0.000 description 4
150000004676 glycans Chemical class 0.000 description 4
230000000977 initiatory effect Effects 0.000 description 4
238000002347 injection Methods 0.000 description 4
239000007924 injection Substances 0.000 description 4
239000007788 liquid Substances 0.000 description 4
229960003128 mupirocin Drugs 0.000 description 4
229930187697 mupirocin Natural products 0.000 description 4
DDHVILIIHBIMQU-YJGQQKNPSA-L mupirocin calcium hydrate Chemical compound O.O.[Ca+2].C[C@H](O)[C@H](C)[C@@H]1O[C@H]1C[C@@H]1[C@@H](O)[C@@H](O)[C@H](C\C(C)=C\C(=O)OCCCCCCCCC([O-])=O)OC1.C[C@H](O)[C@H](C)[C@@H]1O[C@H]1C[C@@H]1[C@@H](O)[C@@H](O)[C@H](C\C(C)=C\C(=O)OCCCCCCCCC([O-])=O)OC1 DDHVILIIHBIMQU-YJGQQKNPSA-L 0.000 description 4
229920001282 polysaccharide Polymers 0.000 description 4
239000005017 polysaccharide Substances 0.000 description 4
230000017854 proteolysis Effects 0.000 description 4
230000002797 proteolythic effect Effects 0.000 description 4
239000008299 semisolid dosage form Substances 0.000 description 4
239000001488 sodium phosphate Substances 0.000 description 4
229910000162 sodium phosphate Inorganic materials 0.000 description 4
239000011550 stock solution Substances 0.000 description 4
RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 4
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
208000034309 Bacterial disease carrier Diseases 0.000 description 3
229920001661 Chitosan Polymers 0.000 description 3
101100364969 Dictyostelium discoideum scai gene Proteins 0.000 description 3
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
241000725303 Human immunodeficiency virus Species 0.000 description 3
RJQXTJLFIWVMTO-TYNCELHUSA-N Methicillin Chemical compound COC1=CC=CC(OC)=C1C(=O)N[C@@H]1C(=O)N2[C@@H](C(O)=O)C(C)(C)S[C@@H]21 RJQXTJLFIWVMTO-TYNCELHUSA-N 0.000 description 3
MSFSPUZXLOGKHJ-UHFFFAOYSA-N Muraminsaeure Natural products OC(=O)C(C)OC1C(N)C(O)OC(CO)C1O MSFSPUZXLOGKHJ-UHFFFAOYSA-N 0.000 description 3
101100364971 Mus musculus Scai gene Proteins 0.000 description 3
108010013639 Peptidoglycan Proteins 0.000 description 3
239000007983 Tris buffer Substances 0.000 description 3
238000002835 absorbance Methods 0.000 description 3
239000008186 active pharmaceutical agent Substances 0.000 description 3
238000004458 analytical method Methods 0.000 description 3
229940041514 candida albicans extract Drugs 0.000 description 3
239000003795 chemical substances by application Substances 0.000 description 3
238000007398 colorimetric assay Methods 0.000 description 3
239000012141 concentrate Substances 0.000 description 3
238000001514 detection method Methods 0.000 description 3
238000009472 formulation Methods 0.000 description 3
210000000987 immune system Anatomy 0.000 description 3
238000001727 in vivo Methods 0.000 description 3
239000004310 lactic acid Substances 0.000 description 3
235000014655 lactic acid Nutrition 0.000 description 3
239000002502 liposome Substances 0.000 description 3
229960003085 meticillin Drugs 0.000 description 3
238000002156 mixing Methods 0.000 description 3
230000035772 mutation Effects 0.000 description 3
239000013642 negative control Substances 0.000 description 3
239000002674 ointment Substances 0.000 description 3
230000003287 optical effect Effects 0.000 description 3
239000008188 pellet Substances 0.000 description 3
239000012466 permeate Substances 0.000 description 3
230000002085 persistent effect Effects 0.000 description 3
239000000725 suspension Substances 0.000 description 3
238000012360 testing method Methods 0.000 description 3
238000013518 transcription Methods 0.000 description 3
230000035897 transcription Effects 0.000 description 3
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 3
239000013598 vector Substances 0.000 description 3
239000012138 yeast extract Substances 0.000 description 3
XJFPXLWGZWAWRQ-UHFFFAOYSA-N 2-[[2-[[2-[[2-[[2-[(2-azaniumylacetyl)amino]acetyl]amino]acetyl]amino]acetyl]amino]acetyl]amino]acetate Chemical compound NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(O)=O XJFPXLWGZWAWRQ-UHFFFAOYSA-N 0.000 description 2
229920001817 Agar Polymers 0.000 description 2
108010001478 Bacitracin Proteins 0.000 description 2
208000035143 Bacterial infection Diseases 0.000 description 2
239000002028 Biomass Substances 0.000 description 2
241000283690 Bos taurus Species 0.000 description 2
241000282472 Canis lupus familiaris Species 0.000 description 2
229920002101 Chitin Polymers 0.000 description 2
101800004419 Cleaved form Proteins 0.000 description 2
241000252203 Clupea harengus Species 0.000 description 2
238000002965 ELISA Methods 0.000 description 2
244000068988 Glycine max Species 0.000 description 2
FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 2
241000124008 Mammalia Species 0.000 description 2
108010069770 N-acetylhexaglycine Proteins 0.000 description 2
NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
239000002202 Polyethylene glycol Substances 0.000 description 2
241000191965 Staphylococcus carnosus Species 0.000 description 2
241000191978 Staphylococcus simulans Species 0.000 description 2
244000057717 Streptococcus lactis Species 0.000 description 2
102000004142 Trypsin Human genes 0.000 description 2
108090000631 Trypsin Proteins 0.000 description 2
206010052428 Wound Diseases 0.000 description 2
HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 2
239000008272 agar Substances 0.000 description 2
BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 2
229910052921 ammonium sulfate Inorganic materials 0.000 description 2
235000011130 ammonium sulphate Nutrition 0.000 description 2
230000003321 amplification Effects 0.000 description 2
238000010171 animal model Methods 0.000 description 2
239000003242 anti bacterial agent Substances 0.000 description 2
229940088710 antibiotic agent Drugs 0.000 description 2
239000012131 assay buffer Substances 0.000 description 2
229960003071 bacitracin Drugs 0.000 description 2
229930184125 bacitracin Natural products 0.000 description 2
CLKOFPXJLQSYAH-ABRJDSQDSA-N bacitracin A Chemical compound C1SC([C@@H](N)[C@@H](C)CC)=N[C@@H]1C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]1C(=O)N[C@H](CCCN)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2N=CNC=2)C(=O)N[C@H](CC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)NCCCC1 CLKOFPXJLQSYAH-ABRJDSQDSA-N 0.000 description 2
208000022362 bacterial infectious disease Diseases 0.000 description 2
230000003115 biocidal effect Effects 0.000 description 2
230000008033 biological extinction Effects 0.000 description 2
150000001875 compounds Chemical class 0.000 description 2
238000010276 construction Methods 0.000 description 2
235000013365 dairy product Nutrition 0.000 description 2
230000000593 degrading effect Effects 0.000 description 2
238000012217 deletion Methods 0.000 description 2
230000037430 deletion Effects 0.000 description 2
238000011026 diafiltration Methods 0.000 description 2
AIUDWMLXCFRVDR-UHFFFAOYSA-N dimethyl 2-(3-ethyl-3-methylpentyl)propanedioate Chemical compound CCC(C)(CC)CCC(C(=O)OC)C(=O)OC AIUDWMLXCFRVDR-UHFFFAOYSA-N 0.000 description 2
201000010099 disease Diseases 0.000 description 2
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
238000004520 electroporation Methods 0.000 description 2
206010014665 endocarditis Diseases 0.000 description 2
239000013604 expression vector Substances 0.000 description 2
230000004927 fusion Effects 0.000 description 2
230000002068 genetic effect Effects 0.000 description 2
238000001631 haemodialysis Methods 0.000 description 2
230000036541 health Effects 0.000 description 2
230000000322 hemodialysis Effects 0.000 description 2
235000019514 herring Nutrition 0.000 description 2
238000007654 immersion Methods 0.000 description 2
238000000338 in vitro Methods 0.000 description 2
239000004615 ingredient Substances 0.000 description 2
NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
238000010255 intramuscular injection Methods 0.000 description 2
239000007927 intramuscular injection Substances 0.000 description 2
238000002955 isolation Methods 0.000 description 2
101150009839 lacF gene Proteins 0.000 description 2
JJTUDXZGHPGLLC-UHFFFAOYSA-N lactide Chemical compound CC1OC(=O)C(C)OC1=O JJTUDXZGHPGLLC-UHFFFAOYSA-N 0.000 description 2
239000008101 lactose Substances 0.000 description 2
210000004185 liver Anatomy 0.000 description 2
239000006210 lotion Substances 0.000 description 2
239000012528 membrane Substances 0.000 description 2
229930182817 methionine Natural products 0.000 description 2
238000007857 nested PCR Methods 0.000 description 2
238000003199 nucleic acid amplification method Methods 0.000 description 2
150000007523 nucleic acids Chemical group 0.000 description 2
230000008520 organization Effects 0.000 description 2
210000001322 periplasm Anatomy 0.000 description 2
238000013492 plasmid preparation Methods 0.000 description 2
229920000747 poly(lactic acid) Polymers 0.000 description 2
229920001467 poly(styrenesulfonates) Polymers 0.000 description 2
229920001223 polyethylene glycol Polymers 0.000 description 2
229920000232 polyglycine polymer Polymers 0.000 description 2
229960002796 polystyrene sulfonate Drugs 0.000 description 2
239000011970 polystyrene sulfonate Substances 0.000 description 2
230000002265 prevention Effects 0.000 description 2
238000012545 processing Methods 0.000 description 2
239000011535 reaction buffer Substances 0.000 description 2
239000012557 regeneration buffer Substances 0.000 description 2
108091008146 restriction endonucleases Proteins 0.000 description 2
238000012216 screening Methods 0.000 description 2
230000003248 secreting effect Effects 0.000 description 2
230000037432 silent mutation Effects 0.000 description 2
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
239000007787 solid Substances 0.000 description 2
238000010561 standard procedure Methods 0.000 description 2
208000015339 staphylococcus aureus infection Diseases 0.000 description 2
238000010254 subcutaneous injection Methods 0.000 description 2
239000007929 subcutaneous injection Substances 0.000 description 2
239000000126 substance Substances 0.000 description 2
239000006228 supernatant Substances 0.000 description 2
230000009885 systemic effect Effects 0.000 description 2
229940124597 therapeutic agent Drugs 0.000 description 2
230000001225 therapeutic effect Effects 0.000 description 2
230000001131 transforming effect Effects 0.000 description 2
230000014621 translational initiation Effects 0.000 description 2
239000012588 trypsin Substances 0.000 description 2
238000011144 upstream manufacturing Methods 0.000 description 2
239000011701 zinc Substances 0.000 description 2
229910052725 zinc Inorganic materials 0.000 description 2
NHJVRSWLHSJWIN-UHFFFAOYSA-N 2,4,6-trinitrobenzenesulfonic acid Chemical compound OS(=O)(=O)C1=C([N+]([O-])=O)C=C([N+]([O-])=O)C=C1[N+]([O-])=O NHJVRSWLHSJWIN-UHFFFAOYSA-N 0.000 description 1
ADBDCISWOGJASO-PROWLMFFSA-N 5-[(3as,4s,6ar)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]pentanoic acid;1-hydroxy-2,5-dioxopyrrolidine-3-sulfonic acid;octanoic acid Chemical compound CCCCCCCC(O)=O.ON1C(=O)CC(S(O)(=O)=O)C1=O.N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 ADBDCISWOGJASO-PROWLMFFSA-N 0.000 description 1
FHVDTGUDJYJELY-UHFFFAOYSA-N 6-{[2-carboxy-4,5-dihydroxy-6-(phosphanyloxy)oxan-3-yl]oxy}-4,5-dihydroxy-3-phosphanyloxane-2-carboxylic acid Chemical compound O1C(C(O)=O)C(P)C(O)C(O)C1OC1C(C(O)=O)OC(OP)C(O)C1O FHVDTGUDJYJELY-UHFFFAOYSA-N 0.000 description 1
208000030507 AIDS Diseases 0.000 description 1
108700042778 Antimicrobial Peptides Proteins 0.000 description 1
102000044503 Antimicrobial Peptides Human genes 0.000 description 1
108010062877 Bacteriocins Proteins 0.000 description 1
VOVIALXJUBGFJZ-KWVAZRHASA-N Budesonide Chemical compound C1CC2=CC(=O)C=C[C@]2(C)[C@@H]2[C@@H]1[C@@H]1C[C@H]3OC(CCC)O[C@@]3(C(=O)CO)[C@@]1(C)C[C@@H]2O VOVIALXJUBGFJZ-KWVAZRHASA-N 0.000 description 1
241000282832 Camelidae Species 0.000 description 1
241000283707 Capra Species 0.000 description 1
208000017667 Chronic Disease Diseases 0.000 description 1
206010053567 Coagulopathies Diseases 0.000 description 1
208000035473 Communicable disease Diseases 0.000 description 1
229920000742 Cotton Polymers 0.000 description 1
206010011409 Cross infection Diseases 0.000 description 1
229920000858 Cyclodextrin Polymers 0.000 description 1
206010011763 Cystic fibrosis lung Diseases 0.000 description 1
230000004543 DNA replication Effects 0.000 description 1
238000001712 DNA sequencing Methods 0.000 description 1
229920002307 Dextran Polymers 0.000 description 1
239000003109 Disodium ethylene diamine tetraacetate Substances 0.000 description 1
206010059866 Drug resistance Diseases 0.000 description 1
ZGTMUACCHSMWAC-UHFFFAOYSA-L EDTA disodium salt (anhydrous) Chemical compound [Na+].[Na+].OC(=O)CN(CC([O-])=O)CCN(CC(O)=O)CC([O-])=O ZGTMUACCHSMWAC-UHFFFAOYSA-L 0.000 description 1
238000012286 ELISA Assay Methods 0.000 description 1
241000196324 Embryophyta Species 0.000 description 1
108010059378 Endopeptidases Proteins 0.000 description 1
102000005593 Endopeptidases Human genes 0.000 description 1
241000283086 Equidae Species 0.000 description 1
241000282326 Felis catus Species 0.000 description 1
206010016654 Fibrosis Diseases 0.000 description 1
241000192125 Firmicutes Species 0.000 description 1
WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
208000031886 HIV Infections Diseases 0.000 description 1
208000037357 HIV infectious disease Diseases 0.000 description 1
241000282412 Homo Species 0.000 description 1
206010061598 Immunodeficiency Diseases 0.000 description 1
102000004877 Insulin Human genes 0.000 description 1
108090001061 Insulin Proteins 0.000 description 1
208000036209 Intraabdominal Infections Diseases 0.000 description 1
DEFJQIDDEAULHB-IMJSIDKUSA-N L-alanyl-L-alanine Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(O)=O DEFJQIDDEAULHB-IMJSIDKUSA-N 0.000 description 1
241000194036 Lactococcus Species 0.000 description 1
241000194034 Lactococcus lactis subsp. cremoris Species 0.000 description 1
102000003960 Ligases Human genes 0.000 description 1
108090000364 Ligases Proteins 0.000 description 1
102000016943 Muramidase Human genes 0.000 description 1
108010014251 Muramidase Proteins 0.000 description 1
241000699670 Mus sp. Species 0.000 description 1
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
108700026244 Open Reading Frames Proteins 0.000 description 1
235000019483 Peanut oil Nutrition 0.000 description 1
241001494479 Pecora Species 0.000 description 1
108091005804 Peptidases Proteins 0.000 description 1
102000035195 Peptidases Human genes 0.000 description 1
239000001888 Peptone Substances 0.000 description 1
108010080698 Peptones Proteins 0.000 description 1
229920001213 Polysorbate 20 Polymers 0.000 description 1
206010067268 Post procedural infection Diseases 0.000 description 1
206010036590 Premature baby Diseases 0.000 description 1
241000288906 Primates Species 0.000 description 1
239000012614 Q-Sepharose Substances 0.000 description 1
238000011152 Q-Sepharose FF chromatography Methods 0.000 description 1
241000700159 Rattus Species 0.000 description 1
102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
241000282849 Ruminantia Species 0.000 description 1
238000012300 Sequence Analysis Methods 0.000 description 1
MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
241000144290 Sigmodon hispidus Species 0.000 description 1
VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
108091081024 Start codon Proteins 0.000 description 1
235000014897 Streptococcus lactis Nutrition 0.000 description 1
241000282887 Suidae Species 0.000 description 1
208000031650 Surgical Wound Infection Diseases 0.000 description 1
240000002670 Tagetes lucida Species 0.000 description 1
235000003591 Tagetes lucida Nutrition 0.000 description 1
241000700605 Viruses Species 0.000 description 1
208000027418 Wounds and injury Diseases 0.000 description 1
HMNZFMSWFCAGGW-XPWSMXQVSA-N [3-[hydroxy(2-hydroxyethoxy)phosphoryl]oxy-2-[(e)-octadec-9-enoyl]oxypropyl] (e)-octadec-9-enoate Chemical compound CCCCCCCC\C=C\CCCCCCCC(=O)OCC(COP(O)(=O)OCCO)OC(=O)CCCCCCC\C=C\CCCCCCCC HMNZFMSWFCAGGW-XPWSMXQVSA-N 0.000 description 1
238000010521 absorption reaction Methods 0.000 description 1
238000009825 accumulation Methods 0.000 description 1
210000001552 airway epithelial cell Anatomy 0.000 description 1
235000004279 alanine Nutrition 0.000 description 1
-1 alanine amino acids Chemical class 0.000 description 1
108010056243 alanylalanine Proteins 0.000 description 1
229940072056 alginate Drugs 0.000 description 1
229920000615 alginic acid Polymers 0.000 description 1
235000010443 alginic acid Nutrition 0.000 description 1
229910000147 aluminium phosphate Inorganic materials 0.000 description 1
150000001412 amines Chemical class 0.000 description 1
229960000723 ampicillin Drugs 0.000 description 1
AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
239000010775 animal oil Substances 0.000 description 1
239000003963 antioxidant agent Substances 0.000 description 1
230000003078 antioxidant effect Effects 0.000 description 1
210000001765 aortic valve Anatomy 0.000 description 1
238000013459 approach Methods 0.000 description 1
PYMYPHUHKUWMLA-WDCZJNDASA-N arabinose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)C=O PYMYPHUHKUWMLA-WDCZJNDASA-N 0.000 description 1
PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 1
239000011324 bead Substances 0.000 description 1
235000015278 beef Nutrition 0.000 description 1
230000009286 beneficial effect Effects 0.000 description 1
230000008901 benefit Effects 0.000 description 1
SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 1
WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
239000000227 bioadhesive Substances 0.000 description 1
230000015572 biosynthetic process Effects 0.000 description 1
238000009640 blood culture Methods 0.000 description 1
229910021538 borax Inorganic materials 0.000 description 1
229960004436 budesonide Drugs 0.000 description 1
210000004899 c-terminal region Anatomy 0.000 description 1
239000001506 calcium phosphate Substances 0.000 description 1
229910000389 calcium phosphate Inorganic materials 0.000 description 1
235000011010 calcium phosphates Nutrition 0.000 description 1
239000002775 capsule Substances 0.000 description 1
238000013132 cardiothoracic surgery Methods 0.000 description 1
238000005277 cation exchange chromatography Methods 0.000 description 1
239000001913 cellulose Substances 0.000 description 1
229920002678 cellulose Polymers 0.000 description 1
238000005119 centrifugation Methods 0.000 description 1
210000001175 cerebrospinal fluid Anatomy 0.000 description 1
RKLXDNHNLPUQRB-TVJUEJKUSA-N chembl564271 Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]1C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]2C(C)SC[C@H](N[C@@H](CC(N)=O)C(=O)NC(=O)[C@@H](NC2=O)CSC1C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)CC)C(=O)NC(=C)C(=O)N[C@@H](CCCCN)C(O)=O)NC(=O)[C@H]1NC(=O)C(=C\C)/NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H]2NC(=O)CNC(=O)[C@@H]3CCCN3C(=O)[C@@H](NC(=O)[C@H]3N[C@@H](CC(C)C)C(=O)NC(=O)C(=C)NC(=O)CC[C@H](NC(=O)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CC=4C5=CC=CC=C5NC=4)CSC3)C(O)=O)C(C)SC2)C(C)C)C(C)SC1)C1=CC=CC=C1 RKLXDNHNLPUQRB-TVJUEJKUSA-N 0.000 description 1
229960005091 chloramphenicol Drugs 0.000 description 1
WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
238000004587 chromatography analysis Methods 0.000 description 1
239000012539 chromatography resin Substances 0.000 description 1
230000002759 chromosomal effect Effects 0.000 description 1
230000001684 chronic effect Effects 0.000 description 1
230000007882 cirrhosis Effects 0.000 description 1
208000019425 cirrhosis of liver Diseases 0.000 description 1
238000003776 cleavage reaction Methods 0.000 description 1
238000012411 cloning technique Methods 0.000 description 1
230000035602 clotting Effects 0.000 description 1
108010055222 clotting enzyme Proteins 0.000 description 1
239000011248 coating agent Substances 0.000 description 1
238000000576 coating method Methods 0.000 description 1
238000004440 column chromatography Methods 0.000 description 1
238000001816 cooling Methods 0.000 description 1
229920001577 copolymer Polymers 0.000 description 1
238000004132 cross linking Methods 0.000 description 1
229940097362 cyclodextrins Drugs 0.000 description 1
230000007423 decrease Effects 0.000 description 1
238000013461 design Methods 0.000 description 1
239000008121 dextrose Substances 0.000 description 1
238000010586 diagram Methods 0.000 description 1
231100000676 disease causative agent Toxicity 0.000 description 1
235000019301 disodium ethylene diamine tetraacetate Nutrition 0.000 description 1
239000002552 dosage form Substances 0.000 description 1
230000008030 elimination Effects 0.000 description 1
238000003379 elimination reaction Methods 0.000 description 1
238000010828 elution Methods 0.000 description 1
239000012149 elution buffer Substances 0.000 description 1
239000002158 endotoxin Substances 0.000 description 1
239000003623 enhancer Substances 0.000 description 1
230000002255 enzymatic effect Effects 0.000 description 1
238000001976 enzyme digestion Methods 0.000 description 1
230000008029 eradication Effects 0.000 description 1
210000003527 eukaryotic cell Anatomy 0.000 description 1
238000011156 evaluation Methods 0.000 description 1
230000005284 excitation Effects 0.000 description 1
239000000284 extract Substances 0.000 description 1
238000000605 extraction Methods 0.000 description 1
229920001002 functional polymer Polymers 0.000 description 1
230000002496 gastric effect Effects 0.000 description 1
238000011902 gastrointestinal surgery Methods 0.000 description 1
239000001963 growth medium Substances 0.000 description 1
210000003709 heart valve Anatomy 0.000 description 1
244000144980 herd Species 0.000 description 1
239000012456 homogeneous solution Substances 0.000 description 1
208000033519 human immunodeficiency virus infectious disease Diseases 0.000 description 1
230000002209 hydrophobic effect Effects 0.000 description 1
230000014726 immortalization of host cell Effects 0.000 description 1
230000036039 immunity Effects 0.000 description 1
239000007943 implant Substances 0.000 description 1
230000006698 induction Effects 0.000 description 1
238000003780 insertion Methods 0.000 description 1
230000037431 insertion Effects 0.000 description 1
229940125396 insulin Drugs 0.000 description 1
230000003914 insulin secretion Effects 0.000 description 1
238000007912 intraperitoneal administration Methods 0.000 description 1
238000007913 intrathecal administration Methods 0.000 description 1
238000001990 intravenous administration Methods 0.000 description 1
238000007914 intraventricular administration Methods 0.000 description 1
238000004255 ion exchange chromatography Methods 0.000 description 1
238000011031 large-scale manufacturing process Methods 0.000 description 1
239000012669 liquid formulation Substances 0.000 description 1
244000144972 livestock Species 0.000 description 1
210000004072 lung Anatomy 0.000 description 1
210000001165 lymph node Anatomy 0.000 description 1
239000006166 lysate Substances 0.000 description 1
229960000274 lysozyme Drugs 0.000 description 1
235000010335 lysozyme Nutrition 0.000 description 1
239000004325 lysozyme Substances 0.000 description 1
230000014759 maintenance of location Effects 0.000 description 1
230000035800 maturation Effects 0.000 description 1
230000007246 mechanism Effects 0.000 description 1
238000001471 micro-filtration Methods 0.000 description 1
239000011859 microparticle Substances 0.000 description 1
239000004005 microsphere Substances 0.000 description 1
235000010446 mineral oil Nutrition 0.000 description 1
239000002480 mineral oil Substances 0.000 description 1
238000010369 molecular cloning Methods 0.000 description 1
239000003068 molecular probe Substances 0.000 description 1
230000003232 mucoadhesive effect Effects 0.000 description 1
210000004877 mucosa Anatomy 0.000 description 1
108010009719 mutanolysin Proteins 0.000 description 1
210000001331 nose Anatomy 0.000 description 1
235000016709 nutrition Nutrition 0.000 description 1
230000035764 nutrition Effects 0.000 description 1
239000003921 oil Substances 0.000 description 1
235000019198 oils Nutrition 0.000 description 1
230000008506 pathogenesis Effects 0.000 description 1
239000000312 peanut oil Substances 0.000 description 1
101150064613 pepN gene Proteins 0.000 description 1
235000019319 peptone Nutrition 0.000 description 1
239000003208 petroleum Substances 0.000 description 1
239000002504 physiological saline solution Substances 0.000 description 1
238000007747 plating Methods 0.000 description 1
108010094020 polyglycine Proteins 0.000 description 1
229920000642 polymer Polymers 0.000 description 1
239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
229920000136 polysorbate Polymers 0.000 description 1
239000013641 positive control Substances 0.000 description 1
230000002980 postoperative effect Effects 0.000 description 1
230000001323 posttranslational effect Effects 0.000 description 1
239000000843 powder Substances 0.000 description 1
238000001556 precipitation Methods 0.000 description 1
230000002028 premature Effects 0.000 description 1
125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
210000001236 prokaryotic cell Anatomy 0.000 description 1
230000000069 prophylactic effect Effects 0.000 description 1
235000019833 protease Nutrition 0.000 description 1
238000001742 protein purification Methods 0.000 description 1
238000011552 rat model Methods 0.000 description 1
238000003259 recombinant expression Methods 0.000 description 1
230000003252 repetitive effect Effects 0.000 description 1
239000011347 resin Substances 0.000 description 1
229920005989 resin Polymers 0.000 description 1
239000012898 sample dilution Substances 0.000 description 1
238000011012 sanitization Methods 0.000 description 1
230000007017 scission Effects 0.000 description 1
238000011218 seed culture Methods 0.000 description 1
230000035945 sensitivity Effects 0.000 description 1
238000013207 serial dilution Methods 0.000 description 1
210000002966 serum Anatomy 0.000 description 1
239000008159 sesame oil Substances 0.000 description 1
235000011803 sesame oil Nutrition 0.000 description 1
239000011734 sodium Substances 0.000 description 1
239000001632 sodium acetate Substances 0.000 description 1
235000017281 sodium acetate Nutrition 0.000 description 1
239000001509 sodium citrate Substances 0.000 description 1
235000010339 sodium tetraborate Nutrition 0.000 description 1
239000003549 soybean oil Substances 0.000 description 1
235000012424 soybean oil Nutrition 0.000 description 1
230000006641 stabilisation Effects 0.000 description 1
238000011105 stabilization Methods 0.000 description 1
230000000087 stabilizing effect Effects 0.000 description 1
229940037648 staphylococcus simulans Drugs 0.000 description 1
238000006467 substitution reaction Methods 0.000 description 1
108010082567 subtilin Proteins 0.000 description 1
238000001356 surgical procedure Methods 0.000 description 1
235000013706 tagetes lucida Nutrition 0.000 description 1
238000002560 therapeutic procedure Methods 0.000 description 1
210000001519 tissue Anatomy 0.000 description 1
230000009466 transformation Effects 0.000 description 1
238000013519 translation Methods 0.000 description 1
238000002054 transplantation Methods 0.000 description 1
QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
BSVBQGMMJUBVOD-UHFFFAOYSA-N trisodium borate Chemical compound [Na+].[Na+].[Na+].[O-]B([O-])[O-] BSVBQGMMJUBVOD-UHFFFAOYSA-N 0.000 description 1
HRXKRNGNAMMEHJ-UHFFFAOYSA-K trisodium citrate Chemical compound [Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O HRXKRNGNAMMEHJ-UHFFFAOYSA-K 0.000 description 1
229940038773 trisodium citrate Drugs 0.000 description 1
238000002255 vaccination Methods 0.000 description 1
235000015112 vegetable and seed oil Nutrition 0.000 description 1
239000008158 vegetable oil Substances 0.000 description 1
239000003981 vehicle Substances 0.000 description 1
231100000747 viability assay Toxicity 0.000 description 1
238000003026 viability measurement method Methods 0.000 description 1
238000003260 vortexing Methods 0.000 description 1
238000005406 washing Methods 0.000 description 1
239000002699 waste material Substances 0.000 description 1

Images

Classifications

- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Engineering & Computer Science (AREA)
Zoology (AREA)
Wood Science & Technology (AREA)
Genetics & Genomics (AREA)
Bioinformatics & Cheminformatics (AREA)
General Health & Medical Sciences (AREA)
Medicinal Chemistry (AREA)
Biochemistry (AREA)
Biomedical Technology (AREA)
General Engineering & Computer Science (AREA)
Microbiology (AREA)
Molecular Biology (AREA)
Biotechnology (AREA)
Oncology (AREA)
Pharmacology & Pharmacy (AREA)
Communicable Diseases (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Veterinary Medicine (AREA)
Animal Behavior & Ethology (AREA)
General Chemical & Material Sciences (AREA)
Chemical Kinetics & Catalysis (AREA)
Public Health (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Peptides Or Proteins (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Enzymes And Modification Thereof (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)

JP2003579727A 2001-12-21 2002-12-23 ブドウ球菌溶解活性が増強された切断型リゾスタフィン分子 Expired - Fee Related JP4348194B2 (ja)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US34180401P	2001-12-21	2001-12-21
PCT/US2002/040924 WO2003082184A2 (en)	2001-12-21	2002-12-23	Truncated lysostaphin molecule with enhanced staphylolytic activity

Publications (2)

Publication Number	Publication Date
JP2005519628A JP2005519628A (ja)	2005-07-07
JP4348194B2 true JP4348194B2 (ja)	2009-10-21

Family

ID=28675229

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP2003579727A Expired - Fee Related JP4348194B2 (ja)	2001-12-21	2002-12-23	ブドウ球菌溶解活性が増強された切断型リゾスタフィン分子

Country Status (7)

Country	Link
US (1)	US20050118159A1 (de)
EP (1)	EP1465990B1 (de)
JP (1)	JP4348194B2 (de)
AT (1)	ATE516356T1 (de)
AU (1)	AU2002367820B2 (de)
CA (1)	CA2469720A1 (de)
WO (1)	WO2003082184A2 (de)

Families Citing this family (26)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
EP1734931A2 (de) *	2004-03-24	2006-12-27	Actavis Group	Formulierungen von ramipril
CN100475965C (zh) *	2005-07-22	2009-04-08	上海高科联合生物技术研发有限公司	一种大肠杆菌高效外分泌表达溶葡萄球菌酶的方法
WO2009114520A2 (en) *	2008-03-10	2009-09-17	Pharmain Corporation	Compositions for treatment with metallopeptidases, methods of making and using the same
WO2015020765A2 (en) *	2013-08-06	2015-02-12	Trustees Of Dartmouth College	Unglycosylated lysostaphin variant protein
WO2015175774A1 (en)	2014-05-14	2015-11-19	Trustees Of Dartmouth College	Deimmunized lysostaphin and methods of use
CN106148254B (zh) *	2015-03-26	2019-11-12	南京华贞生物医药科技有限公司	一种用于减肥降脂的转化体及其构建方法与应用
CN107916244A (zh) *	2017-06-20	2018-04-17	江西嘉博生物工程有限公司	一种表达溶葡球菌素基因的重组乳酸乳球菌的构建方法及应用
JP7460531B2 (ja) *	2017-12-05	2024-04-02	バイオピーエルエックス，インコーポレイティド	微生物感染を防ぐための方法および組成物
CA3171721A1 (en)	2020-03-19	2021-09-23	Fritz Eichenseher	A stabilized protein of interest
CN115976158B (zh) *	2023-03-16	2023-07-04	百葵锐(天津)生物科技有限公司	一种裂解酶酶活性测定方法
WO2024241070A1 (en)	2023-05-22	2024-11-28	L'oreal	Cosmetic composition comprising an endolysin and a polyvinyl alcohol
FR3152395A1 (fr)	2023-08-28	2025-03-07	L'oreal	Composition cosmétique comprenant une endolysine dérivée de phage de Staphylococcus aureus et la 4-hydroxyacetophenone
FR3149207B1 (fr)	2023-06-02	2026-03-13	Oreal	Composition cosmétique comprenant une endolysine et un composé de formule (I)
FR3149203B1 (fr)	2023-06-02	2026-03-13	Oreal	Composition anhydre comprenant une endolysine et de l’hydroxypropylmethylcellulose et/ou du pullulane
EP4719330A1 (de)	2023-06-02	2026-04-08	L'oreal	Kosmetische zusammensetzung mit einem endolysin aus einem staphylococcus-aureus-phagen und einem aromatischen alkohol
FR3149205B1 (fr)	2023-06-02	2026-04-24	Loreal	Composition cosmétique comprenant une endolysine et un agent de charge organique
FR3149204B1 (fr)	2023-06-02	2026-02-13	Oreal	Composition cosmétique comprenant une endolysine et un tensioactif non ionique comprenant un résidu carbohydrate
FR3149208B1 (fr)	2023-06-02	2026-03-20	Oreal	Composition cosmétique, notamment aqueuse, comprenant une endolysine et un pullulane
FR3149202B1 (fr)	2023-06-02	2026-04-10	Oreal	Composition cosmétique comprenant une endolysine dérivée de phage de Staphylococcus aureus et une huile.
FR3149206B1 (fr)	2023-06-02	2026-03-13	Oreal	Composition cosmétique aqueuse comprenant une endolysine et du tréhalose
FR3149209B1 (fr)	2023-06-02	2026-04-03	Oreal	Composition cosmétique comprenant une endolysine dérivée de phage de Staphylococcus aureus et un alcool aromatique
FR3152394B1 (fr)	2023-08-28	2026-04-24	Loreal	Composition cosmétique comprenant une endolysine et des particules d’aérogel de silice hydrophobe
FR3152393B1 (fr)	2023-08-28	2026-04-24	Loreal	Composition cosmétique comprenant une endolysine dérivée d’un phage de Staphylococcus aureus et une charge minérale
FR3152396A1 (fr)	2023-08-28	2025-03-07	L'oreal	Composition cosmétique comprenant une endolysine dérivée de phage de Staphylococcus aureus et un polyhydroxyalcane
WO2025093666A1 (en)	2023-11-01	2025-05-08	University Of Copenhagen	Treatment of lymphoma
WO2026052743A1 (en)	2024-09-04	2026-03-12	Micreos Human Health B.V.	Reduction of trans-epidermal water loss by a polypeptide with antibacterial properties

Family Cites Families (9)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4931390A (en) *	1986-04-16	1990-06-05	Public Health Research Institute Of The City Of New York, Inc.	Expression of the cloned lysostaphin gene
US5011772A (en) *	1988-02-05	1991-04-30	Public Health Research Institute Of The City Of N.Y.	High yield protein production system
DE4425645A1 (de) *	1994-07-20	1996-02-22	Mueller Karl & Co Kg	Deletiertes Lysostaphingen von Staphylococcus simulans
US6028051A (en) *	1997-07-23	2000-02-22	Ambi Inc.	Method for the treatment of staphylococcal disease
CA2211293A1 (en) *	1997-07-23	1999-01-23	Immunova Ltee	Recombinant lysostaphin analogs
US6248558B1 (en) *	1998-03-31	2001-06-19	Vanderbilt University	Sequence and method for genetic engineering of proteins with cell membrane translocating activity
AU4706799A (en) *	1998-06-22	2000-01-10	University Of Vermont And State Agricultural College, The	Treatment of (staphylococcus) infections
MXPA02003885A (es) *	1999-10-19	2005-06-03	Bharat Biotech International L	Expresion de lisostafina madura recombinante.
AU2001256350A1 (en) *	2000-05-12	2001-11-20	Bayer Aktiengesellschaft	Regulation of human lysostaphin-like protease

2002
- 2002-12-23 EP EP02806841A patent/EP1465990B1/de not_active Expired - Lifetime
- 2002-12-23 CA CA002469720A patent/CA2469720A1/en not_active Abandoned
- 2002-12-23 AT AT02806841T patent/ATE516356T1/de not_active IP Right Cessation
- 2002-12-23 WO PCT/US2002/040924 patent/WO2003082184A2/en not_active Ceased
- 2002-12-23 US US10/499,690 patent/US20050118159A1/en not_active Abandoned
- 2002-12-23 JP JP2003579727A patent/JP4348194B2/ja not_active Expired - Fee Related
- 2002-12-23 AU AU2002367820A patent/AU2002367820B2/en not_active Ceased

Also Published As

Publication number	Publication date
AU2002367820B2 (en)	2007-11-01
CA2469720A1 (en)	2003-10-09
EP1465990A2 (de)	2004-10-13
WO2003082184A2 (en)	2003-10-09
ATE516356T1 (de)	2011-07-15
EP1465990A4 (de)	2006-06-28
JP2005519628A (ja)	2005-07-07
AU2002367820A1 (en)	2003-10-13
US20050118159A1 (en)	2005-06-02
EP1465990B1 (de)	2011-07-13
WO2003082184A3 (en)	2004-07-22

Legal Events

Date	Code	Title	Description
2005-12-08	A621	Written request for application examination	Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20051207
2009-01-14	A131	Notification of reasons for refusal	Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20090113
2009-04-14	A521	Request for written amendment filed	Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20090413
2009-06-15	TRDD	Decision of grant or rejection written
2009-06-24	A01	Written decision to grant a patent or to grant a registration (utility model)	Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20090623
2009-06-25	A01	Written decision to grant a patent or to grant a registration (utility model)	Free format text: JAPANESE INTERMEDIATE CODE: A01
2009-07-23	A61	First payment of annual fees (during grant procedure)	Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20090717
2009-07-24	R150	Certificate of patent or registration of utility model	Free format text: JAPANESE INTERMEDIATE CODE: R150
2009-07-27	FPAY	Renewal fee payment (event date is renewal date of database)	Free format text: PAYMENT UNTIL: 20120724 Year of fee payment: 3
2012-07-24	LAPS	Cancellation because of no payment of annual fees

Publication	Publication Date	Title
JP4348194B2 (ja)	2009-10-21	ブドウ球菌溶解活性が増強された切断型リゾスタフィン分子
JP6587655B2 (ja)	2019-10-09	グラム陽性細菌を検出および処置するためのＳｔｒｅｐｔｏｃｏｃｃｕｓバクテリオファージリシン
EP3010932B1 (de)	2017-07-19	Bakterielle hyaluronidase und verfahren zu deren herstellung
JP2023103347A (ja)	2023-07-26	血液成分による溶菌タンパク質の抗菌活性の強化、並びにその方法及び使用
JP2014519485A (ja)	2014-08-14	コンパニオン動物および家畜におけるグラム陽性細菌を処置するためのＳｔｒｅｐｔｏｃｏｃｃｕｓバクテリオファージリシン
AU2018203076B2 (en)	2020-03-19	Dimeric bacteriophage lysins
HK1260296B (en)	2021-04-23	Dimeric bacteriophage lysins
HK1260296A1 (en)	2019-12-13	Dimeric bacteriophage lysins
HK1259586A1 (en)	2019-11-29	Dimeric bacteriophage lysins
HK1203549B (en)	2019-07-26	Dimeric bacteriophage lysins